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UnknownA Concise, Modular Antibody-Oligonucleotide Conjugation Strategy Based on Disuccinimidyl Ester Activation Chemistry.
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S-EPMC6773266 | biostudies-literature
ProteomicsDSSBU: An MS-Cleavable Analogue of the BS3 Cross-Linker
In this study, we introduce a new MS-cleavable cross-linker called disulfodisuccinimidyl dibutyric urea (DSSBU), which we developed in-house. DSSBU contains an N-hydroxysulfosuccinimide (sulfo-NHS) reactive group that primarily modifies lysine residues. It therefore serves as a water-soluble counter...
ORGANISM(S): Bos taurus (Bovine) 
2025-12-29 | PXD052450 | Pride
Bsa Protein cross-linking Dssbu cross-linker 
ProteomicspH dependence of succinimide ester-based protein cross-linking for structural mass spectrometry applications
The pH dependency of the reaction of the cross-linking reagent, disuccinimidyl suberate (DSS), was studied on a set of eight model proteins.
ORGANISM(S): Bos taurus (Bovine) Oryctolagus cuniculus (Rabbit) Gallus gallus (Chicken) 
2021-11-15 | PXD027891 | Pride
Chemical cross-linking  dss  model proteins  method optimization  ph dependency 
ProteomicsComparison of DSS and DSSO workflows
Disuccinimidyl suberate (DSS) and disuccinimidyl sulfoxide (DSSO) exemplify these two strategies, respectively. Conventional wisdom suggests that DSS is optimal for simple samples, while DSSO excels in complex proteomes. However, this widespread assumption lacks rigorous, systematic validation. Here...
ORGANISM(S): Homo Sapiens Escherichia Coli Saccharomyces Cerevisiae 
2025-12-01 | PXD071417 |
ProteomicsA hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT
Chemical cross-linking coupled to mass spectrometry was used to study assembly intermediates of the chaperonin TRiC/CCT. Complex were cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2023-08-24 | PXD043532 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding  chaperonin  tric/cct 
ProteomicsCharacterization of Integrator module INTS10-INTS13-INTS14 and its connection to the cleavage module Part I
Chemical cross-linking coupled to mass spectrometry was used to study the complex between the Integrator complex subunits INTS13 (Asunder) and INTS14. Cross-linking was performed using disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2020-06-18 | PXD015682 | Pride
Chemical cross-linking  dss  structural proteomics  integrator complex 
ProteomicsPuf6 ushers correct rRNA compaction during ribosome assembly
Chemical cross-linking coupled to mass spectrometry was used to study the complex between the nucleolar factor, Puf6, and the yeast 60S ribosome. Disuccinimidyl suberate (DSS) was used as the cross-linking reagent.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-06-28 | PXD024131 | Pride
Chemical cross-linking  dss  structural proteomics  ribosome  ribosomal assembly 
ProteomicsThe TRiC Chaperonin and Prefoldin Cooperate to Fold and Assemble Viral Capsid Oligomers
Chemical cross-linking coupled to mass spectrometry was used to study the folding of the reovirus sigma3 protein by the chaperonin, TRiC/CCT. Cross-linking was performed using the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2021-02-04 | PXD019751 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding Tric/cct chaperonin 
ProteomicsCross-linking mass spectrometry of a complex between the chaperonin TRiC/CCT and its cochaperones, prefoldin and phosducin-like protein 2A
Chemical cross-linking coupled to mass spectrometry was used to study the architecture of the co-complex between TRiC/CCT, PFD and PhLP2A. The complex was cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).
ORGANISM(S): Homo sapiens (Human) 
2023-12-11 | PXD040144 | Pride
Chemical cross-linking  dss  structural proteomics  protein folding  chaperonin  tric/cct  prefoldin  phosducin-like protein 2a 
ProteomicsPhosphorylation of TRAIP is essential for mitotic replisome disassembly and MiDAS
Chemical cross-linking coupled to mass spectrometry was used to study the structure and homodimerization of the E3 ubiquitin ligase TRAIP from Xenopus laevis. The protein was cross-linked with two different concentrations of disuccinimidyl suberate (DSS).
ORGANISM(S): Xenopus laevis (African clawed frog) 
2025-06-27 | PXD058941 | Pride
Chemical cross-linking  dss  traip 
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